CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1100
Functional Family

Enzyme Information

4.2.1.22
Cystathionine beta-synthase.
based on mapping to UniProt Q9YBL2
L-serine + L-homocysteine = L-cystathionine + H(2)O.
-!- A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta- substituted alpha-L-amino acids and a variety of mercaptans. -!- Formerly EC 4.2.1.21.
2.5.1.47
Cysteine synthase.
based on mapping to UniProt Q9YBL2
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.
-!- Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. -!- Not identical with EC 2.5.1.51, EC 2.5.1.52 and EC 2.5.1.53. -!- Formerly EC 4.2.99.8.
2.5.1.65
O-phosphoserine sulfhydrylase.
based on mapping to UniProt Q9YBL2
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate.
-!- The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O(3)-acetyl-L-serine, in contrast with EC 2.5.1.47, which acts only on O(3)-acetyl-L-serine.

UniProtKB Entries (1)

Q9YBL2
CYSO_AERPE
Aeropyrum pernix K1
Protein CysO

PDB Structure

PDB 3VSA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1
Nakamura, T., Kawai, Y., Kunimoto, K., Iwasaki, Y., Nishii, K., Kataoka, M., Ishikawa, K.
J.Mol.Biol.